Applications: |
Immunodepletion/Immunocompetition |
Note: |
STRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS. |
Short Description: |
CARD15 Blocking Peptide for STJ501934 is synthetically produced from the 700-780 sequence and is suitable for use in western blot applications. |
Formulation: |
Liquid form at 2.5mg/ml concentration in PBS. Up to 5% DMSO can be added. Orders with >1mg can be supplied in lyophilized powder form, or in buffer of choice. |
Storage Instruction: |
Store at-20°C for long term storage. Avoid freeze-thaw cycles. |
Gene Symbol: |
Nod2Uniprot ID=NOD2_MOUSE" |
Immunogen Region: |
700-780 |
Specificity: |
This blocking peptide is recommended for use in combination with CARD15 antibody, STJ501934 |
Immunogen: |
Synthetic peptide taken within amino acid region 700-780 on mouse Nucleotide-binding oligomerization domain-containing protein 2. |
Tissue Specificity | Expressed in monocytes, macrophages, dendritic cells, hepatocytes, preadipocytes, epithelial cells of oral cavity, lung and intestine. In intestine, highly expressed in ileal Paneth cells of the crypt and in intestinal stem cells. Also expressed in neurons of several brain regions including the hypothalamus. |
Post Translational Modifications | Palmitoylated by ZDHHC5.palmitoylation is required for proper recruitment to the bacterial entry site and hence for proper signaling upon cognate peptidoglycan detection. Palmitoylation promotes localization to the cell membrane. Palmitoylation protects from SQSTM1/p62-dependent autophagic degradation. Polyubiquitinated by TRIM27, leading to proteasome-mediated degradation. Polyubiquitinated and degraded following muramyl dipeptide (MDP) stimulation, conferring MDP tolerance and preventing septic shock. Degraded via selective autophagy following interaction with Irgm1. Irgm1 promotes NOD2-RIPK2 RIPosome recruitment to autophagosome membranes, promoting their SQSTM1/p62-dependent autophagic degradation. O-glycosylated by OGT, O-GlcNAcylation increases protein stability. |
Function | Pattern recognition receptor (PRR) that detects bacterial peptidoglycan fragments and other danger signals and plays an important role in gastrointestinal immunity. Specifically activated by muramyl dipeptide (MDP), a fragment of bacterial peptidoglycan found in every bacterial peptidoglycan type. NOD2 specifically recognizes and binds 6-O-phospho-MDP, the phosphorylated form of MDP, which is generated by NAGK. 6-O-phospho-MDP-binding triggers oligomerization that facilitates the binding and subsequent activation of the proximal adapter receptor-interacting RIPK2. Following recruitment, RIPK2 undergoes 'Met-1'- (linear) and 'Lys-63'-linked polyubiquitination by E3 ubiquitin-protein ligases XIAP, BIRC2, BIRC3 and the LUBAC complex, becoming a scaffolding protein for downstream effectors, triggering activation of the NF-kappa-B and MAP kinases signaling. This in turn leads to the transcriptional activation of hundreds of genes involved in immune response. Its ability to detect bacterial MDP plays a central role in maintaining the equilibrium between intestinal microbiota and host immune responses to control inflammation. An imbalance in this relationship results in dysbiosis, whereby pathogenic bacteria prevail on commensals, causing damage in the intestinal epithelial barrier as well as allowing bacterial invasion and inflammation. Acts as a regulator of appetite by sensing MDP in a subset of brain neurons: microbiota-derived MDP reach the brain, where they bind and activate NOD2 in inhibitory hypothalamic neurons, decreasing neuronal activity, thereby regulating satiety and body temperature. NOD2-dependent MDP-sensing of bacterial cell walls in the intestinal epithelial compartment contributes to sustained postnatal growth upon undernutrition. Also plays a role in antiviral response by acting as a sensor of single-stranded RNA (ssRNA) from viruses: upon ssRNA-binding, interacts with MAVS, leading to activation of interferon regulatory factor-3/IRF3 and expression of type I interferon. Also acts as a regulator of autophagy in dendritic cells via its interaction with ATG16L1, possibly by recruiting ATG16L1 at the site of bacterial entry. NOD2 activation in the small intestine crypt also contributes to intestinal stem cells survival and function: acts by promoting mitophagy via its association with ATG16L1. In addition to its main role in innate immunity, also regulates the adaptive immune system by acting as regulator of helper T-cell and regulatory T-cells (Tregs). Besides recognizing pathogens, also involved in the endoplasmic reticulum stress response: acts by sensing and binding to the cytosolic metabolite sphingosine-1-phosphate generated in response to endoplasmic reticulum stress, initiating an inflammation process that leads to activation of the NF-kappa-B and MAP kinases signaling. May also be involved in NLRP1 activation following activation by MDP, leading to CASP1 activation and IL1B release in macrophages. |
Peptide Name | Nucleotide-Binding Oligomerization Domain-Containing Protein 2Caspase Recruitment Domain-Containing Protein 15 |
Cellular Localisation | Cell MembraneLipid-AnchorBasolateral Cell MembraneCytoplasmMitochondrionPalmitoylation Promotes Localization To The Cell MembraneWhere It Detects Bacterial Invasion At The Point Of Entry |
Alternative Peptide Names | Nucleotide-Binding Oligomerization Domain-Containing Protein 2 proteinCaspase Recruitment Domain-Containing Protein 15 proteinNod2 proteinCard15 protein |
Information sourced from Uniprot.org
12 months for antibodies. 6 months for ELISA Kits. Please see website T&Cs for further guidance